ID D9Q038_ACIS3 Unreviewed; 459 AA. AC D9Q038; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 26-FEB-2020, entry version 62. DE RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000256|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=ASAC_0269 {ECO:0000313|EMBL:ADL18676.1}; OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / OS 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18676.1, ECO:0000313|Proteomes:UP000000346}; RN [1] {ECO:0000313|EMBL:ADL18676.1, ECO:0000313|Proteomes:UP000000346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15 RC {ECO:0000313|Proteomes:UP000000346}; RX PubMed=20581186; DOI=10.1128/AEM.00599-10; RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports RT a new order, Acidilobales, and suggests an important ecological role in RT terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able CC to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- CC seryl-tRNA(Sec), which will be further converted into selenocysteinyl- CC tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L- CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742, CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00176}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L- CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00176}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. CC {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N- CC terminal extension that is involved in tRNA binding. CC {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00176}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001742; ADL18676.1; -; Genomic_DNA. DR RefSeq; WP_013266188.1; NC_014374.1. DR STRING; 666510.ASAC_0269; -. DR EnsemblBacteria; ADL18676; ADL18676; ASAC_0269. DR GeneID; 9498492; -. DR KEGG; asc:ASAC_0269; -. DR eggNOG; arCOG00403; Archaea. DR eggNOG; COG0172; LUCA. DR HOGENOM; CLU_023797_0_1_2; -. DR KO; K01875; -. DR OMA; SPCFRRE; -. DR OrthoDB; 16385at2157; -. DR BioCyc; ASAC666510:G1GMD-285-MONOMER; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000346; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00770; SerRS_core; 1. DR Gene3D; 1.10.287.40; -; 1. DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002317; Ser-tRNA-ligase_type_1. DR InterPro; IPR015866; Ser-tRNA-synth_1_N. DR InterPro; IPR042103; SerRS_1_N_sf. DR InterPro; IPR033729; SerRS_core. DR InterPro; IPR010978; tRNA-bd_arm. DR PANTHER; PTHR11778; PTHR11778; 1. DR Pfam; PF02403; Seryl_tRNA_N; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 2. DR PRINTS; PR00981; TRNASYNTHSER. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00414; serS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176, KW ECO:0000313|EMBL:ADL18676.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:ADL18676.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}. FT DOMAIN 164..433 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" FT NP_BIND 284..286 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" FT NP_BIND 371..374 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" FT REGION 253..255 FT /note="Serine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" FT COILED 33..53 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 69..103 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 300 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" FT BINDING 307 FT /note="Serine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" FT BINDING 408 FT /note="Serine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" SQ SEQUENCE 459 AA; 52780 MW; D59E1563610261A4 CRC64; MPWSILNLLR TNPEALREVA RKRQIDVKII DEAVQLDEQW RKVQAEINEL RHQHNVISAA IPKAKGEERE KLLAQAKELS RELEDAERRL SELEAKREEA LWRLPNVVLD DVPVGGEEAT RPVRFWGTPR VYHEYLDAFK AQTEAYGFNV PYELIDWKPV GHADMLENVL KLGDTEKASE VAGSRFYYLF DDLVWLDFAL LLYAIDKLTS KGYTLVLPPY MLRYKVINSV IDLATFQDAI YKIENDDLYL IATAEHSLAA MYYNEELYDD ELPKKFVGIS PAFRREAGAA NKDLKGIFRV HQFHKVEQFV FSKPEESQKI HEELISNAEG LFQGLGIPYR VVNIASGDLG ACAVKKYDLE AWMPAQGKYR EMVSASNCTD WQAYRLNIRL IRRKGMERGE YVHTLNSTGI ASTRTITAIL ENFQEPDGTV IIPKVLRKYL EPFDAAPKDF IKPRPRKAI //